MolNFT v1 · #104964 · protein
Human HMT1 hnrnp methyltransferase-like protein 6 (S. cerevisiae) with gms
4QQK · Protein arginine N-methyltransferase 6: “Human HMT1 hnrnp methyltransferase-like protein 6 (S. cerevisiae) with gms”. X-ray diffraction, 2 ligands (37H, UNX), 2 pockets (best druggability 0.59). MolNFT v1 #104964 on GenesisL1: 3D…
- PDB
- 4QQK
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein arginine N-methyltransferase 6
- EC
- 2.1.1.-, 2.1.1.125
- UniProt
- Q96LA8
- Ligands
- 37H, UNX
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arginine N-methyltransferase 6 (EC 2.1.1.-, 2.1.1.125) | protein | 324 | 30% helix, 37% strand | Q96LA8 |
Ligands and binding sites
- 37H · (5S)-5-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}-N~6~-carbamimidoyl-L-lysine · ligand · chains A
- UNX · Unknown atom or ion · ion · 21 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.59 | 0.79 | 38 | 37H, UNX |
| 2 | 141 | 0.58 | 0.83 | 19 | UNX |
Compared structures
- 4QQK · Human HMT1 hnRNP methyltransferase-like protein 6 (S. cerevisiae) with GMS · the same entry in another collection · chain A against A, TM-score 1.00
- Q96LA8 · AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 6 (Q96LA8) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q96LA8
- Elsewhere: RCSB PDB 4QQK · PDBe 4QQK · UniProt Q96LA8
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